{"database":"iProX","file_versions":[],"scores":null,"additional":{"omics_type":["Proteomics"],"submitter":["Chun Liu"],"species":["Bombyx Mori"],"full_dataset_link":["http://www.iprox.org/page/project.html?id=IPX0013361000"],"submitter_email":["mlliuchun@163.com"],"submitter_affiliation":["State Key Laboratory of Resource Insects, Southwest University"],"sample_protocol":[""],"repository":["iProX"],"data_protocol":[""],"additional_accession":[]},"is_claimable":false,"name":"Activity Identification and Proteomics Analysis of Water-Soluble  Proteins in Cocoon Coat from Different Silkworm Varieties","description":"This study established, for the first time, a system for extracting water-soluble active proteins from the cocoon layers of multiple pigmented silkworm varieties and systematically evaluated their consistent antioxidant activities together with variety-specific antimicrobial functions. DIA-based proteomics identified 462 catalytic and binding proteins, revealing compositional differences among the three varieties and demonstrating that active protein diversity underlies the observed divergence in antimicrobial efficacy. Differential protein analysis highlighted zonadhesin-like proteins as key components, with TIL domains predicted by AlphaFold 3 to form a unique convex loop-mediated interaction interface. This work provides the first evidence of high-abundance insect-derived zonadhesin-like proteins in the cocoon matrix, and although their functional roles remain uncharacterized, the finding establishes a novel direction for future mechanistic research.","dates":{"publication":"Mon Mar 30 00:00:00 BST 2026"},"accession":"PXD076347","cross_references":{"TAXONOMY":["7091"]}}